Essential structural elements in tRNAPro for EF-P-mediated alleviation of translation stalling

Abstract The ribosome stalls on translation of polyproline sequences due to inefficient peptide bond formation between consecutive prolines. The translation factor EF-P is able to alleviate this stalling by accelerating Pro-Pro formation. However, the mechanism by which EF-P recognizes the stalled c...

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Bibliographic Details
Published inNature communications Vol. 7; no. 1; pp. 11657 - 12
Main Authors Katoh, Takayuki, Wohlgemuth, Ingo, Nagano, Masanobu, Rodnina, Marina V., Suga, Hiroaki
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group 24.05.2016
Nature Portfolio
Subjects
Amino acids
E coli
Enzymes
Peptides
Proteins
Ribonucleic acid
RNA
Transfer RNA
Yeast
Japan
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Summary:Abstract The ribosome stalls on translation of polyproline sequences due to inefficient peptide bond formation between consecutive prolines. The translation factor EF-P is able to alleviate this stalling by accelerating Pro-Pro formation. However, the mechanism by which EF-P recognizes the stalled complexes and accelerates peptide bond formation is not known. Here, we use genetic code reprogramming through a flexible in-vitro translation (FIT) system to investigate how mutations in tRNA Pro affect EF-P function. We show that the 9-nt D-loop closed by the stable D-stem sequence in tRNA Pro is a crucial recognition determinant for EF-P. Such D-arm structures are shared only among the tRNA Pro isoacceptors and tRNA fMet in Escherichia coli , and the D-arm of tRNA fMet is essential for EF-P-induced acceleration of fMet–puromycin formation. Thus, the activity of EF-P is controlled by recognition elements in the tRNA D-arm.
ISSN:2041-1723
2041-1723
DOI:10.1038/ncomms11657